The effect of myoglobin concentration on aerobic dive limit in a Weddell seal

Wright, Traver J.; Davis, Randall W.

doi:10.1242/jeb.02273

Cited by 15 publications

(9 citation statements)

References 41 publications

(53 reference statements)

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“…Skeletal muscles of humans and small animals living at high altitude exhibit a more than tenfold higher concentration of myoglobin as also observed for diving mammals and birds compared with non-diving species at sea level (Kanatous et al, 2008;Kooyman and Ponganis, 1998). The muscle myoglobin content of diving mammals is regulated by their diving behavior and directly correlates with the dive type and duration (Kanatous et al, 2008;Wright and Davis, 2006). Additional adaptations like promotion of angiogenesis, vascular remodeling and mitochondrial volume density are coordinated by increased hypoxiainducible factor (HIF-1) activation.…”

Section: The Role Of Myoglobin In Hypoxic-induced Angiogenesismentioning

confidence: 91%

Unmasking the Janus face of myoglobin in health and disease

Hendgen‐Cotta

Flögel

Kelm

et al. 2010

Journal of Experimental Biology

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SummaryFor more than 100 years, myoglobin has been among the most extensively studied proteins. Since the first comprehensive review on myoglobin function as a dioxygen store by Millikan in 1939 and the discovery of its structure 50 years ago, multiple studies have extended our understanding of its occurrence, properties and functions. Beyond the two major roles, the storage and the facilitation of dioxygen diffusion, recent physiological studies have revealed that myoglobin acts as a potent scavenger of nitric oxide (NO • ) representing a control system that preserves mitochondrial respiration. In addition, myoglobin may also protect the heart against reactive oxygen species (ROS), and, under hypoxic conditions, deoxygenated myoglobin is able to reduce nitrite to NO • leading to a downregulation of the cardiac energy status and to a decreased heart injury after reoxygenation. Thus, by controlling the NO • bioavailability via scavenging or formation, myoglobin serves as part of a sensitive dioxygen sensory system. In this review, the physiological relevance of these recent findings are delineated for pathological states where NO • and ROS bioavailability are known to be critical determinants for the outcome of the disease, e.g. ischemia/reperfusion injury. Detrimental and beneficial effects of the presence of myoglobin are discussed for various states of tissue oxygen tension within the heart and skeletal muscle. Furthermore, the impact of myoglobin on parasite infection, rhabdomyolysis, hindlimb and liver ischemia, angiogenesis and tumor growth are considered.

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Section: The Role Of Myoglobin In Hypoxic-induced Angiogenesismentioning

confidence: 91%

Unmasking the Janus face of myoglobin in health and disease

Hendgen‐Cotta

Flögel

Kelm

et al. 2010

Journal of Experimental Biology

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“…Despite low arterial oxygen content, oxygen supply to muscle mitochondria is normally maintained by endogenous oxygen stores (MbO 2 ) and convective oxygen transport to maintain aerobic metabolism (Wright and Davis, 2006). Vasoconstriction in diving vertebrates reduces convective oxygen transport to muscle tissues and oxygen supply is further reduced as arterial P O2 drops throughout the dive.…”

Section: Globin Adaptation To Hypoxiamentioning

confidence: 99%

“…The concentration of Mb in the skeletal muscle of birds and mammals varies greatly among species. In air-breathing diving vertebrates, high concentrations of Mb serve as an oxygen store for periods of regional muscle hypoxia during prolonged apnea (Guyton et al, 1995;Ponganis et al, 1997b;Wright and Davis, 2006;Davis, 2014) and may represent as much as 50% of total oxygen store (Butler and Jones, 1997). While many terrestrial mammals have Mb concentrations <5 mg g −1 muscle tissue (Newcom et al, 2004;Masuda et al, 2008), Mb concentration in diving mammals is often 10-fold greater (Kanatous and Mammen, 2010) with some concentrations exceeding 78 mg g −1 (Noren and Williams, 2000).…”

Section: Introductionmentioning

confidence: 99%

Myoglobin oxygen affinity in aquatic and terrestrial birds and mammals

Wright

Davis

2015

Journal of Experimental Biology

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Myoglobin (Mb) is an oxygen binding protein found in vertebrate skeletal muscle, where it facilitates intracellular transport and storage of oxygen. This protein has evolved to suit unique physiological needs in the muscle of diving vertebrates that express Mb at much greater concentrations than their terrestrial counterparts. In this study, we characterized Mb oxygen affinity (P 50 ) from 25 species of aquatic and terrestrial birds and mammals. Among diving species, we tested for correlations between Mb P 50 and routine dive duration. Across all species examined, Mb P 50 ranged from 2.40 to 4.85 mmHg. The mean P 50 of Mb from terrestrial ungulates was 3.72±0.15 mmHg (range 3.70-3.74 mmHg). The P 50 of cetaceans was similar to terrestrial ungulates ranging from 3.54 to 3.82 mmHg, with the exception of the melonheaded whale, which had a significantly higher P 50 of 4.85 mmHg. Among pinnipeds, the P 50 ranged from 3.23 to 3.81 mmHg and showed a trend for higher oxygen affinity in species with longer dive durations. Among diving birds, the P 50 ranged from 2.40 to 3.36 mmHg and also showed a trend of higher affinities in species with longer dive durations. In pinnipeds and birds, low Mb P 50 was associated with species whose muscles are metabolically active under hypoxic conditions associated with aerobic dives. Given the broad range of potential globin oxygen affinities, Mb P 50 from diverse vertebrate species appears constrained within a relatively narrow range. High Mb oxygen affinity within this range may be adaptive for some vertebrates that make prolonged dives.

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“…It is striking that some cetacean species have acquired an ability to echolocate that has enabled them to use sound to locate prey or escape obstacles when navigating (Cranford et al 1996). Moreover, cetaceans have elevated levels of myoglobin in their skeletal muscles (Noren et al 2001; Wright and Davis 2006), which vastly increases their ability to retain oxygen, allowing for longer time between breaths. They also use glycolysis metabolism to compensate for insufficient levels of oxygen (Butler and Jones 1997), which potentially supports the energy supply for their long dives.…”

Section: Introductionmentioning

confidence: 99%

Genome-Wide Scans for Candidate Genes Involved in the Aquatic Adaptation of Dolphins

Sun

Zhou

Liu

et al. 2012

Genome Biology and Evolution

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Since their divergence from the terrestrial artiodactyls, cetaceans have fully adapted to an aquatic lifestyle, which represents one of the most dramatic transformations in mammalian evolutionary history. Numerous morphological and physiological characters of cetaceans have been acquired in response to this drastic habitat transition, such as thickened blubber, echolocation, and ability to hold their breath for a long period of time. However, knowledge about the molecular basis underlying these adaptations is still limited. The sequence of the genome of Tursiops truncates provides an opportunity for a comparative genomic analyses to examine the molecular adaptation of this species. Here, we constructed 11,838 high-quality orthologous gene alignments culled from the dolphin and four other terrestrial mammalian genomes and screened for positive selection occurring in the dolphin lineage. In total, 368 (3.1%) of the genes were identified as having undergone positive selection by the branch-site model. Functional characterization of these genes showed that they are significantly enriched in the categories of lipid transport and localization, ATPase activity, sense perception of sound, and muscle contraction, areas that are potentially related to cetacean adaptations. In contrast, we did not find a similar pattern in the cow, a closely related species. We resequenced some of the positively selected sites (PSSs), within the positively selected genes, and showed that most of our identified PSSs (50/52) could be replicated. The results from this study should have important implications for our understanding of cetacean evolution and their adaptations to the aquatic environment.

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The effect of myoglobin concentration on aerobic dive limit in a Weddell seal

Cited by 15 publications

References 41 publications

Unmasking the Janus face of myoglobin in health and disease

Unmasking the Janus face of myoglobin in health and disease

Myoglobin oxygen affinity in aquatic and terrestrial birds and mammals

Genome-Wide Scans for Candidate Genes Involved in the Aquatic Adaptation of Dolphins

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